ArticleThe Journal of biological chemistry2004
The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently.
Article in The Journal of biological chemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 102 citations in OpenAlex.
- Hepatitis C virus NS3 helicase contributes to (-) strand RNA synthesis.Nature communications · 2025Article
- Dual function of Zika virus NS2B-NS3 protease.PLoS pathogens · 2023Article
- Flavivirus proteases: The viral Achilles heel to prevent future pandemics.Antiviral research · 2023Review
- Mechanical regulation of the helicase activity of Zika virus NS3.Biophysical journal · 2022Article
- Characterization of a multipurpose NS3 surface patch coordinating HCV replicase assembly and virion morphogenesis.PLoS pathogens · 2022Article
- Recombinant HCV NS3 and NS5B enzymes exhibit multiple posttranslational modifications for potential regulation.Virus genes · 2019Article
- New Techniques to Study Intracellular Receptors in Living Cells: Insights Into RIG-I-Like Receptor Signaling.Advances in experimental medicine and biology · 2019Review
- NS3 from Hepatitis C Virus Strain JFH-1 Is an Unusually Robust Helicase That Is Primed To Bind and Unwind Viral RNA.Journal of virology · 2018Article
- Uncoupling of ProteaseJournal of virology · 2017Article
- Quantitative microspectroscopic imaging reveals viral and cellular RNA helicase interactions in live cells.The Journal of biological chemistry · 2017Article
- Article
- The Spring α-Helix Coordinates Multiple Modes of HCV (Hepatitis C Virus) NS3 Helicase Action.The Journal of biological chemistry · 2016Article
- Simultaneously Targeting the NS3 Protease and Helicase Activities for More Effective Hepatitis C Virus Therapy.ACS chemical biology · 2015Article
- Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand Junction.Biochemistry · 2015Article
- Protease Inhibitors Block Multiple Functions of the NS3/4A Protease-Helicase during the Hepatitis C Virus Life Cycle.Journal of virology · 2015Article
- Nonstructural protein 5A (NS5A) and human replication protein A increase the processivity of hepatitis C virus NS5B polymerase activity in vitro.Journal of virology · 2015Article
- The intraviral protein interaction network of hepatitis C virus.Molecular & cellular proteomics : MCP · 2014Article
- Amodiaquine, an antimalarial drug, inhibits dengue virus type 2 replication and infectivity.Antiviral research · 2014Article
- Functional interplay among the flavivirus NS3 protease, helicase, and cofactors.Virologica Sinica · 2014Review
- Functional cross-talk between distant domains of chikungunya virus non-structural protein 2 is decisive for its RNA-modulating activity.The Journal of biological chemistry · 2014Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The nonstructural 3 (NS3) protein encoded by the hepatitis C virus possesses both an N-terminal serine protease activity and a C-terminal 3'-5' helicase activity. This study examines the effects of the protease on the helicase by comparing the enzymatic properties of the full-length NS3 protein with truncated versions in which the protease is either deleted or replaced by a polyhistidine (His tag) or a glutathione S-transferase fusion protein (GST tag). When the NS3 protein lacks the protease domain it unwinds RNA more slowly and does not unwind RNA in the presence of excess nucleic acid that acts as an enzyme trap. Some but not all of the RNA helicase activity can be restored by adding a His tag or GST tag to the N terminus of the truncated helicase, suggesting that the effects of the protease are both specific and nonspecific. Similar but smaller effects are also seen in DNA helicase and translocation assays. While translocating on RNA (or DNA) the full-length protein hydrolyzes ATP more slowly than the truncated protein, suggesting that the protease allows for more efficient ATP usage. Binding assays reveal that the full-length protein assembles on single-stranded DNA as a higher order oligomer than the truncated fragment, and the binding appears to be more cooperative. The data suggest that hepatitis C virus RNA helicase, and therefore viral replication, could be influenced by the rotations of the protease domain which likely occur during polyprotein processing.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.